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Mapping the folding landscape of green fluorescent proteins

NSF Award:

Topics in Protein Folding and Dynamics  (University of Maryland College Park)

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The discovery of green fluorescent protein (GFP) garnered the 2008 Nobel Prize in Chemistry. Now GFP is widely used to visualize complex cellular processes in biotechnology and cell biology. Because GFP and related fluorescent proteins are large molecules and possess complex architectures, researchers have found mapping their folding action a challenge.

However, the development of computer simulations using an alternative theoretical approach now makes it possible to quantitatively map the sequence of complex parallel events that lead the protein from an expanded, unfolded shape to a barrel-like, folded state. The simulations replicate experimental thermodynamic and kinetic data on large proteins. The work opens new ways of describing how large proteins, which play a vital role in cell signaling, reach their functional states.

The simulations also provide a way to tweak the complex folding pathways. These options could have profound benefits in biotechnology and molecular biology studies. From a basic scientific perspective, this research illustrates the successful simulation of large proteins. Such an advance ushers in a new era in which researchers can begin to understand the interactions between biological molecules that drive a variety of cellular processes.

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  • the folding landscape of green fluorescent protein
The folding landscape of green fluorescent protein.
D. Thirumalai, University of Maryland

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